2vd5 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Dystrophia myotonica protein kinase (DMPK) is a serine/threonine kinase composed of a kinase domain and a coiled-coil domain involved in the multimerization. The crystal structure of the kinase domain of DMPK bound to the inhibitor bisindolylmaleimide VIII (BIM-8) revealed a dimeric enzyme associated by a conserved dimerization domain. The affinity of dimerisation suggested that the kinase domain alone is insufficient for dimerisation in vivo and that the coiled-coil domains are required for stable dimer formation. The kinase domain is in an active conformation, with a fully-ordered and correctly positioned alphaC helix, and catalytic residues in a conformation competent for catalysis. The conserved hydrophobic motif at the C-terminal extension of the kinase domain is bound to the N-terminal lobe of the kinase domain, despite being unphosphorylated. Differences in the arrangement of the C-terminal extension compared to the closely related Rho-associated kinases include an altered PXXP motif, a different conformation and binding arrangement for the turn motif, and a different location for the conserved NFD motif. The BIM-8 inhibitor occupies the ATP site and has similar binding mode as observed in PDK1.
Structure of dystrophia myotonica protein kinase.,Elkins JM, Amos A, Niesen FH, Pike AC, Fedorov O, Knapp S Protein Sci. 2009 Apr;18(4):782-91. PMID:19309729[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Elkins JM, Amos A, Niesen FH, Pike AC, Fedorov O, Knapp S. Structure of dystrophia myotonica protein kinase. Protein Sci. 2009 Apr;18(4):782-91. PMID:19309729 doi:10.1002/pro.82
